ID   G0S4V9_CHATD            Unreviewed;       831 AA.
AC   G0S4V9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
GN   ORFNames=CTHT_0031850 {ECO:0000313|EMBL:EGS21330.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS21330.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001657};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; GL988041; EGS21330.1; -; Genomic_DNA.
DR   RefSeq; XP_006693626.1; XM_006693563.1.
DR   AlphaFoldDB; G0S4V9; -.
DR   GeneID; 18257223; -.
DR   KEGG; cthr:CTHT_0031850; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_005043_1_0_1; -.
DR   OMA; FNTWHYG; -.
DR   OrthoDB; 5486960at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06595; GH31_u1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF89; ALPHA-XYLOSIDASE; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EGS21330.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   DOMAIN          191..497
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          505..596
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   REGION          630..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  95138 MW;  24A0F67D557D67C5 CRC64;
     MADRYSFPCK PEANPKAIVT GGSSDSYYRF TVLTERLLRF EWSKDGGFED RVSTFALFRW
     FETPQYQIVD KKDSLQIITD FFHLTYDKKK FSSSGLTVKV GNDVWSYDGN CYGDLGGTTR
     TLDGAYGRVK LEPGVLSRKA YAVLDDSKSM LFENGWIATR VPGRIDGYLF AYHGDHKAAI
     KDFYRLSGNQ PILPRWTLGN WWSRYHAYSA DEYLELMDRF KSEGIPLTVA VIDMDWHKVN
     IPPQYGSGWT GYSWNRELFP DPNGFLSELH KRNLKVTLND HPADGIRSFE DQYELVAKAL
     GHDTSKGEPI RFDCCDRKFL DAYFDVLKLN LEKQGVDFWW IDWQQGTRSR IPGVDPLWVL
     NHYHYLTSRR NIKVLEQPIT FSRYAGPGSH RYPIGFSGDT QITWAGLEFQ PEFTATASNI
     GYGWWSHDIG GHWGGVRSNQ LMVRWVQLGC FSPILRLHSS KNLWNSREPW KYETTAHQII
     KNFLILRHRL IPYLYTMNIR ASYEGEPLIQ PMYWNHTDNE AYTVPTQYYF GTSLIVVPIT
     SPQNATTLLG SVRAWLPRGR FVDIFNPQLV YDGDRYIQLH RDLSHIPVLA KEGTIIPLDG
     NPKLTNGAAR PTEITLLLVV GADAHFELVE EPDTSDHGSK NSQPPLSSFS RTPLNWNQKS
     GILTIGPEWK GTGCWRQWTV KLVGHTNTNV QARVPGFRVT QDENSTTICL GNVHRWNPDG
     FEIFLGEDLQ LDVVDVKARV FERIHKAEME YEAKDSVWDA VSDRSGDKIQ RRVERLMGTN
     VSAALKNAVM EVWAADGRSE GSAKGHEVWA DRTCEPDDDE LDEVLKDYII V
//